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Structural insights into the mechanism of adaptive ribosomal modification by Pseudomonas RimK

DOI: 10.1002/prot.26429 DOI Help

Authors: Catriona M. A. Thompson (John Innes Centre; University of East Anglia) , Richard H. Little (John Innes Centre) , Clare E. M. Stevenson (John Innes Centre) , David M. Lawson (John Innes Centre) , Jacob G. Malone (John Innes Centre; University of East Anglia)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Proteins: Structure, Function, And Bioinformatics

State: Published (Approved)
Published: September 2022
Diamond Proposal Number(s): 13467

Abstract: Bacteria are equipped with a diverse set of regulatory tools that allow them to quickly adapt to their environment. The RimK system allows for Pseudomonas spp. to adapt through post-transcriptional regulation by altering the ribosomal subunit RpsF. RimK is found in a wide range of bacteria with a conserved amino acid sequence, however the genetic context and the role of this protein is highly diverse. By solving and comparing the structures of RimK homologues from two related but functionally divergent systems, we uncovered key structural differences that likely contribute to the different activity levels of each of these homologues. Moreover, we were able to clearly resolve the active site of this protein for the first time, resolving binding of the glutamate substrate. This work advances our understanding of how subtle differences in protein sequence and structure can have profound effects on protein activity, which can in turn result in widespread mechanistic changes.

Journal Keywords: Pseudomonas; Crystal structure; Protein-ligand interaction; Protein-protein interaction; Protein binding; Docking modelling

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography

Added On: 26/09/2022 15:38

Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)